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Literature summary for 1.1.98.6 extracted from

  • Torrents, E.; Eliasson, R.; Wolpher, H.; Graeslund, A.; Reichard, P.
    The anaerobic ribonucleotide reductase from Lactococcus lactis. Interactions between the two proteins NrdD and NrdG (2001), J. Biol. Chem., 276, 33488-33494.
    View publication on PubMed
Search for more literature for 1.1.98.6

Activating Compound

Activating Compound Comment Organism Structure
ATP 1.5 mM, 500fold increase in reduction rate of CTP, 2.5fold increase for GTP Lactococcus cremoris
dGTP 1.5 mM, 20fold increase in reduction rate of ATP Lactococcus cremoris
dTTP 1.5 mM, 3fold increase in reduction rate of GTP Lactococcus cremoris
additional information allosteric effectors bind to two separate sites on NrdD, one binding dATP, dGTP, and dTTP and the other binding dATP and ATP. The two sites show an unusually high degree of cooperativity with complex interactions between effectors and a fine-tuning of their physiological effects Lactococcus cremoris

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Lactococcus cremoris

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
84100
-
-
 Lactococcus cremoris

Organism

Organism UniProt Comment Textmining
Lactococcus cremoris Q9ZAX6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + formate
-
 Lactococcus cremoris dATP + CO2 + H2O
-
 ?
CTP + formate
-
 Lactococcus cremoris dCTP + CO2 + H2O reaction requires both proteins NrdD and NrdG and occurs in two strictly anaerobic steps. During the first step NrdD is activated by S-adenosylmethionine and deazaflavin plus light in a time-dependent reaction. In the second step the actual reduction of CTP by activated NrdD requires dithiothreitol, formate, KCl, and ATP ?
GTP + formate
-
 Lactococcus cremoris dGTP + CO2 + H2O
-
 ?
additional information no substrate: CDP Lactococcus cremoris ?
-
 ?

Subunits

Subunits Comment Organism
? x * 84100, calculated, x * 74000 and x * 84000, due to truncation of protein at the site of the glycyl radical, SDS-PAGE Lactococcus cremoris

Synonyms

Synonyms Comment Organism
anaerobic ribonucleotide reductase
-
 Lactococcus cremoris
nrdD
-
 Lactococcus cremoris

General Information

General Information Comment Organism
physiological function protein NrdD contains catalytic and allosteric sites and, in its active form, a stable glycyl radical. This radical is generated by NrdG with its [4Fe-4S] cluster and S-adenosylmethionine. NrdD and NrdG anaerobically form a tight alpha2beta2 complex. NrdD alone catalyzes the reduction of CTP with formate as the electron donor and ATP as the allosteric effector. The reaction requires Mg+ and is stimulated by K+ but not by dithiothreitol. NrdD is the actual reductase, and NrdG is an activase Lactococcus cremoris
physiological function proteins NrdG and NrdD together catalyze the reduction of ribonucleoside triphosphates to the corresponding deoxyribonucleotides in the presence of S-adenosylmethionine, reduced flavodoxin or reduced deazaflavin, potassium ions, dithiothreitol, and formate. A [4Fe-4S] cluster is present in reduced NrdG and a glycyl radical in activated NrdD. The two polypeptides of NrdD and the proteins in the NrdD-NrdG complex are only loosely associated. NrdDG is required for strict anaerobic growth of Lactococcus lactis Lactococcus cremoris